NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Intermolecular
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233
Intramolecular
Cysteine 138 and cysteine 139
Cysteine 203 and cysteine 233
Cysteine 139 and cysteine 203
Cysteine 138 and cysteine 203
Cysteine 138 and cysteine 233
Cysteine 139 and cysteine 233
7vxu B 152 C 166
A redox-regulated disulphide may form between cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (152 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
42
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
7
Half-sphere exposure sum ?
91
Minimum pKa ?
10
% buried
100
Peptide A name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Peptide B name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Peptide A accession
A0A4X1SVK9
Peptide B accession
A0A4X1VTL7
Peptide A residue number
179
Peptide B residue number
233
Ligandability
Cysteine 179 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu B 155 C 166
A redox-regulated disulphide may form between cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial and cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (155 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
34
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
8
Half-sphere exposure sum ?
96
Minimum pKa ?
10
% buried
100
Peptide A name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Peptide B name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Peptide A accession
A0A4X1SVK9
Peptide B accession
A0A4X1VTL7
Peptide A residue number
182
Peptide B residue number
233
Ligandability
Cysteine 182 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 71 C 72
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 138 and 139 (71 and 72 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
54
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
4
Half-sphere exposure sum ?
89
Minimum pKa ?
14
% buried
nan
Peptide accession
A0A4X1VTL7
Residue number A
138
Residue number B
139
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 138 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 139 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 136 C 166
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 203 and 233 (136 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
50
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
96
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1VTL7
Residue number A
203
Residue number B
233
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 203 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 72 C 136
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 139 and 203 (72 and 136 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
49
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
89
Minimum pKa ?
12
% buried
100
Peptide accession
A0A4X1VTL7
Residue number A
139
Residue number B
203
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 139 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 203 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 71 C 136
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 138 and 203 (71 and 136 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
91
Minimum pKa ?
12
% buried
nan
Peptide accession
A0A4X1VTL7
Residue number A
138
Residue number B
203
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 138 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 203 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 71 C 166
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 138 and 233 (71 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
48
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
94
Minimum pKa ?
10
% buried
nan
Peptide accession
A0A4X1VTL7
Residue number A
138
Residue number B
233
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 138 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
7vxu C 72 C 166
A redox-regulated disulphide may form within NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial between cysteines 139 and 233 (72 and 166 respectively in this structure). However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?
Details
Redox score ?
47
PDB code
7vxu
Structure name
matrix arm of deactive state ci from q10 dataset
Structure deposition date
2021-11-13
Thiol separation (Å)
6
Half-sphere exposure sum ?
93
Minimum pKa ?
10
% buried
100
Peptide accession
A0A4X1VTL7
Residue number A
139
Residue number B
233
Peptide name
NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Ligandability
Cysteine 139 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
Cysteine 233 of NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial
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